Header list of 1a6b.pdb file
Complete list - b 16 2 Bytes
HEADER VIRAL PROTEIN/DNA 23-FEB-98 1A6B
TITLE NMR STRUCTURE OF THE COMPLEX BETWEEN THE ZINC FINGER PROTEIN NCP10 OF
TITLE 2 MOLONEY MURINE LEUKEMIA VIRUS AND A SEQUENCE OF THE PSI-PACKAGING
TITLE 3 DOMAIN OF HIV-1, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*AP*CP*GP*CP*C)-3');
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: ZINC FINGER PROTEIN NCP10;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: CENTRAL DOMAIN RESIDUES 14-53;
COMPND 9 SYNONYM: MOMULV;
COMPND 10 ENGINEERED: YES;
COMPND 11 OTHER_DETAILS: ONE ZINC ION BOUND IN CCHC BOX
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2
KEYWDS NUCLEOCAPSID PROTEIN, INTERCALATION, NUCLEIC ACID, RETROVIRUS, ZINC
KEYWDS 2 FINGER, VIRAL PROTEIN-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.SCHUELER,C.-Z.DONG,K.WECKER,B.P.ROQUES
REVDAT 5 16-FEB-22 1A6B 1 REMARK LINK
REVDAT 4 24-FEB-09 1A6B 1 VERSN
REVDAT 3 01-APR-03 1A6B 1 JRNL
REVDAT 2 02-NOV-99 1A6B 1 JRNL
REVDAT 1 23-AUG-99 1A6B 0
JRNL AUTH W.SCHULER,C.DONG,K.WECKER,B.P.ROQUES
JRNL TITL NMR STRUCTURE OF THE COMPLEX BETWEEN THE ZINC FINGER PROTEIN
JRNL TITL 2 NCP10 OF MOLONEY MURINE LEUKEMIA VIRUS AND THE
JRNL TITL 3 SINGLE-STRANDED PENTANUCLEOTIDE D(ACGCC): COMPARISON WITH
JRNL TITL 4 HIV-NCP7 COMPLEXES.
JRNL REF BIOCHEMISTRY V. 38 12984 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10529168
JRNL DOI 10.1021/BI990378D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.DEMENE,N.JULLIAN,N.MORELLET,H.DE ROCQUIGNY,F.CORNILLE,
REMARK 1 AUTH 2 B.MAIGRET,B.P.ROQUES
REMARK 1 TITL THREE-DIMENSIONAL 1H NMR STRUCTURE OF THE NUCLEOCAPSID
REMARK 1 TITL 2 PROTEIN NCP10 OF MOLONEY MURINE LEUKEMIA VIRUS
REMARK 1 REF J.BIOMOL.NMR V. 4 153 1994
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE PROTEIN PART OF THE STRUCTURE WAS
REMARK 3 GENERATED IN A SIMULATED ANNEALING CALCULATION AND DOCKED WITH
REMARK 3 THE NUCLEOTIDE (IDEALIZED CONFORMATION) IN SUCCESSIVE ENERGY
REMARK 3 MINIMIZATIONS APPLYING FIRST INTRA, THEN INTERMOLECULAR NOE
REMARK 3 RESTRAINTS. THE CONFORMATION OF THE SINGLE STRANDED NUCLEOTIDE
REMARK 3 GETS DEFINED BY THE CONTACTS TO THE PROTEIN. FIFTY STRUCTURES OF
REMARK 3 THE COMPLEX WERE GENERATED BY SIMULATED ANNEALING AND ENERGY
REMARK 3 MINIMIZATION (MAXIMUM GRADIENT O.O2 KCAL/MOL/A2) THE NUCLEOTIDE
REMARK 3 CONFORMATION WAS KEPT FIXED DURING SIMULATED ANNEALING IN THE
REMARK 3 CONFORMATION OBTAINED IN THE FIRST STEP. TWENTY STRUCTURES WERE
REMARK 3 SELECTED WITH RESPECT TO RESTRAINT VIOLATIONS AND TOTAL ENERGY.
REMARK 4
REMARK 4 1A6B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170446.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; E.COSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR, BIOSYM/MSI
REMARK 210 FELIX FELIX
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING,
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS,
REMARK 210 LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: REPRESENTATIVE MODEL NUMBER: ZINC WAS ADDED IN 1.5EQ AS
REMARK 210 ZNCL2. THE STRUCTURE WAS DETERMINED USING 1H-NMR SPECTROSCOPY ON
REMARK 210 THE CENTRAL DOMAIN (14-53)NCP10.
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 DA A 1 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 1 DC A 2 O4' - C1' - N1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 1 DG A 3 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 1 DC A 4 O4' - C1' - N1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 DC A 5 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 DA A 1 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 2 DC A 2 O4' - C1' - N1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 2 DG A 3 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 DC A 4 O4' - C1' - N1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 2 DC A 5 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 2 PRO B 49 CA - N - CD ANGL. DEV. = -11.4 DEGREES
REMARK 500 3 DA A 1 C4' - C3' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 3 DA A 1 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 3 DC A 2 O4' - C1' - N1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 3 DG A 3 O4' - C1' - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 DG A 3 C3' - O3' - P ANGL. DEV. = 7.7 DEGREES
REMARK 500 3 DC A 4 O4' - C1' - N1 ANGL. DEV. = 8.6 DEGREES
REMARK 500 4 DA A 1 C4' - C3' - C2' ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 DA A 1 O4' - C1' - N9 ANGL. DEV. = 5.2 DEGREES
REMARK 500 4 DC A 2 O4' - C1' - N1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 4 DG A 3 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 4 DG A 3 C3' - O3' - P ANGL. DEV. = 7.3 DEGREES
REMARK 500 4 DC A 4 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 LYS B 32 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 5 DA A 1 C1' - O4' - C4' ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 DA A 1 O4' - C1' - N9 ANGL. DEV. = 7.2 DEGREES
REMARK 500 5 DC A 2 O4' - C4' - C3' ANGL. DEV. = -3.6 DEGREES
REMARK 500 5 DC A 2 O4' - C1' - N1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 5 DG A 3 O4' - C1' - N9 ANGL. DEV. = 5.2 DEGREES
REMARK 500 5 DG A 3 C3' - O3' - P ANGL. DEV. = 7.2 DEGREES
REMARK 500 5 DC A 4 O4' - C1' - N1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 5 LYS B 32 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 6 DA A 1 O4' - C1' - N9 ANGL. DEV. = 2.2 DEGREES
REMARK 500 6 DC A 2 O4' - C1' - N1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 6 DG A 3 O4' - C1' - N9 ANGL. DEV. = 4.3 DEGREES
REMARK 500 6 DC A 4 O4' - C1' - C2' ANGL. DEV. = -5.2 DEGREES
REMARK 500 6 DC A 4 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 7 DA A 1 C4' - C3' - C2' ANGL. DEV. = -4.3 DEGREES
REMARK 500 7 DA A 1 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 7 DC A 2 O4' - C1' - N1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 7 DG A 3 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 7 DC A 4 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 8 DA A 1 C4' - C3' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 8 DC A 2 O4' - C1' - N1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 8 DG A 3 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 8 DC A 4 O4' - C1' - N1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 8 PRO B 49 CA - N - CD ANGL. DEV. = -9.7 DEGREES
REMARK 500 9 DC A 2 O4' - C1' - N1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 9 DG A 3 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 9 DC A 4 O4' - C1' - N1 ANGL. DEV. = 6.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 106 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 LYS B 32 -117.38 29.85
REMARK 500 1 ARG B 47 17.22 -162.87
REMARK 500 1 GLN B 52 -46.92 -179.36
REMARK 500 2 GLN B 20 -154.25 -151.32
REMARK 500 2 LYS B 32 -113.84 33.68
REMARK 500 2 PRO B 43 27.00 -64.75
REMARK 500 2 ARG B 44 69.59 60.77
REMARK 500 2 PRO B 49 58.43 37.00
REMARK 500 2 ARG B 50 95.97 42.04
REMARK 500 3 GLU B 15 -78.79 63.87
REMARK 500 3 LEU B 21 93.07 60.46
REMARK 500 3 TYR B 28 -54.13 -127.93
REMARK 500 3 PRO B 49 49.37 -92.37
REMARK 500 4 ASP B 22 -154.27 -147.59
REMARK 500 4 ARG B 23 -75.66 -40.49
REMARK 500 4 ALA B 27 48.28 -83.97
REMARK 500 4 TYR B 28 -53.68 -158.65
REMARK 500 4 LYS B 32 -66.77 -27.32
REMARK 500 4 HIS B 34 -158.20 -156.50
REMARK 500 4 ARG B 47 -67.59 70.62
REMARK 500 4 GLN B 52 -51.32 78.55
REMARK 500 5 GLU B 15 -104.83 -93.79
REMARK 500 5 SER B 19 -150.56 56.08
REMARK 500 5 GLN B 20 -73.03 -129.38
REMARK 500 5 ARG B 23 -75.75 -48.84
REMARK 500 5 TYR B 28 -54.69 -150.04
REMARK 500 5 LYS B 32 -63.76 -27.10
REMARK 500 5 PRO B 43 106.07 -49.84
REMARK 500 5 ARG B 44 67.56 -155.56
REMARK 500 5 ARG B 47 -48.18 -152.62
REMARK 500 6 ARG B 16 -57.02 75.21
REMARK 500 6 ARG B 17 -126.24 65.73
REMARK 500 6 SER B 19 -66.44 -157.50
REMARK 500 6 ASP B 22 -155.48 -93.14
REMARK 500 6 ALA B 27 46.09 -101.10
REMARK 500 6 TYR B 28 -48.49 -166.23
REMARK 500 6 CYS B 39 112.00 -27.23
REMARK 500 7 GLU B 15 99.45 67.31
REMARK 500 7 ARG B 17 -120.51 56.10
REMARK 500 7 ALA B 27 46.22 -83.49
REMARK 500 7 TYR B 28 -51.67 -168.85
REMARK 500 7 CYS B 39 126.76 -34.83
REMARK 500 7 GLN B 52 177.45 62.08
REMARK 500 8 ASP B 22 -150.94 57.41
REMARK 500 8 ALA B 27 48.47 -77.63
REMARK 500 8 TYR B 28 -53.21 -169.91
REMARK 500 8 LYS B 30 55.45 39.69
REMARK 500 8 CYS B 39 113.66 -31.64
REMARK 500 8 ARG B 44 50.60 -155.55
REMARK 500 8 PRO B 49 55.54 32.58
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 DG A 3 0.11 SIDE CHAIN
REMARK 500 2 DG A 3 0.07 SIDE CHAIN
REMARK 500 2 DC A 5 0.07 SIDE CHAIN
REMARK 500 3 DG A 3 0.06 SIDE CHAIN
REMARK 500 4 DG A 3 0.07 SIDE CHAIN
REMARK 500 4 ARG B 23 0.10 SIDE CHAIN
REMARK 500 6 DG A 3 0.11 SIDE CHAIN
REMARK 500 6 DC A 4 0.09 SIDE CHAIN
REMARK 500 7 DG A 3 0.08 SIDE CHAIN
REMARK 500 8 DG A 3 0.09 SIDE CHAIN
REMARK 500 8 DC A 4 0.07 SIDE CHAIN
REMARK 500 9 DG A 3 0.10 SIDE CHAIN
REMARK 500 9 DC A 4 0.07 SIDE CHAIN
REMARK 500 10 DG A 3 0.10 SIDE CHAIN
REMARK 500 11 TYR B 28 0.08 SIDE CHAIN
REMARK 500 12 DG A 3 0.06 SIDE CHAIN
REMARK 500 13 DG A 3 0.08 SIDE CHAIN
REMARK 500 13 ARG B 17 0.08 SIDE CHAIN
REMARK 500 14 DG A 3 0.07 SIDE CHAIN
REMARK 500 15 DG A 3 0.08 SIDE CHAIN
REMARK 500 15 DC A 4 0.12 SIDE CHAIN
REMARK 500 16 DG A 3 0.07 SIDE CHAIN
REMARK 500 17 DG A 3 0.10 SIDE CHAIN
REMARK 500 17 DC A 4 0.07 SIDE CHAIN
REMARK 500 18 DG A 3 0.10 SIDE CHAIN
REMARK 500 18 DC A 4 0.07 SIDE CHAIN
REMARK 500 19 DG A 3 0.12 SIDE CHAIN
REMARK 500 20 DG A 3 0.08 SIDE CHAIN
REMARK 500 20 DC A 4 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 55 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 26 SG
REMARK 620 2 CYS B 29 SG 115.4
REMARK 620 3 HIS B 34 NE2 106.1 106.5
REMARK 620 4 CYS B 39 SG 108.8 110.4 109.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZNB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: ZINC BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 55
DBREF 1A6B B 14 53 UNP P03332 GAG_MLVMO 492 531
DBREF 1A6B A 1 5 PDB 1A6B 1A6B 1 5
SEQRES 1 A 5 DA DC DG DC DC
SEQRES 1 B 40 GLY GLU ARG ARG ARG SER GLN LEU ASP ARG ASP GLN CYS
SEQRES 2 B 40 ALA TYR CYS LYS GLU LYS GLY HIS TRP ALA LYS ASP CYS
SEQRES 3 B 40 PRO LYS LYS PRO ARG GLY PRO ARG GLY PRO ARG PRO GLN
SEQRES 4 B 40 THR
HET ZN B 55 1
HETNAM ZN ZINC ION
FORMUL 3 ZN ZN 2+
LINK SG CYS B 26 ZN ZN B 55 1555 1555 2.31
LINK SG CYS B 29 ZN ZN B 55 1555 1555 2.28
LINK NE2 HIS B 34 ZN ZN B 55 1555 1555 2.02
LINK SG CYS B 39 ZN ZN B 55 1555 1555 2.30
SITE 1 ZNB 4 CYS B 26 CYS B 29 HIS B 34 CYS B 39
SITE 1 AC1 4 CYS B 26 CYS B 29 HIS B 34 CYS B 39
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 16 2 Bytes